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Chromatin dynamics and the RNA exosome function in concert to regulate transcriptional homeostasis (ChIP-seq)

ABSTRACT: The histone variant H2A.Z is a hallmark of nucleosomes flanking the promoters of protein coding genes, and is often found in nucleosomes that also carry lysine 56- acetylated histone H3 (H3-K56Ac), a mark which promotes rapid replication- independent turnover of nucleosomes. Although H2A.Z and H3-K56Ac have been generally implicated in transcriptional activation, their exact contributions have remained elusive. Here we find that H3-K56Ac promotes RNA polymerase II occupancy at a large number of protein coding and noncoding loci, yet neither H3- K56Ac nor H2A.Z has a significant impact on steady state mRNA levels in yeast. Instead, broad effects of H3-K56Ac or H2A.Z on levels of both coding and noncoding RNAs (ncRNAs) are only revealed in the absence of the nuclear RNA exosome. H2A.Z is also necessary for expression of divergent, promoter-proximal ncRNAs in mouse embryonic stem cells, suggesting a conserved role for H2A.Z across eukaryotes. Finally, we show that H2A.Z functions with H3-K56Ac in chromosome folding, facilitating formation of chromosome interaction domains (CIDs). Our study suggests that H2A.Z and H3-K56Ac work in concert with the RNA exosome to control mRNA and ncRNA expression, perhaps in part by regulating higher order chromatin structures. 2 replicates of WT (CY1089), rtt109â (CY2210), rrp6â (CY2071) and one replicate of the W303 input (Sample 7). TableS5.xlsx contains the processed IP/input values for each ORF transcript.

ORGANISM(S): Saccharomyces cerevisiae

SUBMITTER: Craig Peterson

PROVIDER: E-GEOD-72692 | biostudies-arrayexpress |

REPOSITORIES: biostudies-arrayexpress

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Chromatin dynamics and the RNA exosome function in concert to regulate transcriptional homeostasis

Project description:The histone variant H2A.Z is a hallmark of nucleosomes flanking the promoters of protein coding genes, and is often found in nucleosomes that also carry lysine 56- acetylated histone H3 (H3-K56Ac), a mark which promotes rapid replication- independent turnover of nucleosomes. Although H2A.Z and H3-K56Ac have been generally implicated in transcriptional activation, their exact contributions have remained elusive. Here we find that H3-K56Ac promotes RNA polymerase II occupancy at a large number of protein coding and noncoding loci, yet neither H3- K56Ac nor H2A.Z has a significant impact on steady state mRNA levels in yeast. Instead, broad effects of H3-K56Ac or H2A.Z on levels of both coding and noncoding RNAs (ncRNAs) are only revealed in the absence of the nuclear RNA exosome. H2A.Z is also necessary for expression of divergent, promoter-proximal ncRNAs in mouse embryonic stem cells, suggesting a conserved role for H2A.Z across eukaryotes. Finally, we show that H2A.Z functions with H3-K56Ac in chromosome folding, facilitating formation of chromosome interaction domains (CIDs). Our study suggests that H2A.Z and H3-K56Ac work in concert with the RNA exosome to control mRNA and ncRNA expression, perhaps in part by regulating higher order chromatin structures.

2015-10-02 | GSE72845 | GEO

Genome-wide profiling of total RNA from mutants that affect chromatin dynamics: RTT109, SWR1, and the nuclear RNA exosome RRP6

2015-11-12 | GSE73110 | GEO

Chromatin dynamics and the RNA exosome function in concert to regulate transcriptional homeostasis (ChIP-seq)

2015-11-12 | GSE72692 | GEO

Histone H3 lysine 56 acetylation is linked to the core transcriptional network in human embryonic stem cells

Project description:Lysine 56 acetylation in the helical core of histone H3 opens yeast chromatin and enables histone gene transcription, DNA replication, DNA repair, and prevents epigenetic silencing. While K56Ac is globally abundant in yeast and flies its presence has been uncertain in mammals. We show here using mass spectrometry and genome wide analyses that K56Ac is present in human embryonic stem cells (hESCs) overlapping strongly at active and inactive promoters with the binding of the key regulators of pluripotency NANOG, SOX2 and OCT4. This includes also the canonical histone gene promoters and those for the hESC-specific microRNAs. K56Ac then relocates to developmental genes upon cellular differentiation. Thus K56Ac state more accurately reflects the epigenetic differences between hESCs and somatic cells than other active histone marks such as H3 K4 tri-methylation and K9 acetylation. These results suggest that K56Ac is involved in the human core transcriptional network of pluripotency. Genome wide location analysis ChIP-chip was performed in two human embryonic stem cell lines (HSF1 and HSF6) and two somatic cell lines (ARPE and BJ), for each of the following histone modifications: H3 K56Ac, H3 K9Ac, H3 K4me3 and H3 K27me3.

2009-02-09 | E-GEOD-14749 | biostudies-arrayexpress

A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme

Project description:The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function. H2A.Z deposition is controlled by SWR-C chromatin remodeling enzymes that catalyze the nucleosomal exchange of canonical H2A with H2A.Z. Here we report that acetylation of histone H3 lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange where either H2A.Z or H2A can be exchanged from nucleosomes. This result is confirmed in vivo, where genome-wide analysis demonstrates widespread decreases in H2A.Z levels in yeast mutants with hyperacetylated H3K56. Our work also suggests that a conserved SWR-C subunit may function as a M-bM-^@M-^\lockM-bM-^@M-^] that prevents removal of H2A.Z from nucleosomes. Our study identifies a histone modification that regulates a chromatin remodeling reaction and provides insights into how histone variants and nucleosome turnover can be controlled by chromatin regulators. H2A.Z ChIP seq experiments in mutants with constitutive H3K56ac

2013-04-15 | E-GEOD-43935 | biostudies-arrayexpress

A histone acetylation switch regulates H2A.Z deposition by the SWR-C remodeling enzyme

Project description:The histone variant H2A.Z plays key roles in gene expression, DNA repair, and centromere function. H2A.Z deposition is controlled by SWR-C chromatin remodeling enzymes that catalyze the nucleosomal exchange of canonical H2A with H2A.Z. Here we report that acetylation of histone H3 lysine 56 (H3-K56Ac) alters the substrate specificity of SWR-C, leading to promiscuous dimer exchange where either H2A.Z or H2A can be exchanged from nucleosomes. This result is confirmed in vivo, where genome-wide analysis demonstrates widespread decreases in H2A.Z levels in yeast mutants with hyperacetylated H3K56. Our work also suggests that a conserved SWR-C subunit may function as a “lock” that prevents removal of H2A.Z from nucleosomes. Our study identifies a histone modification that regulates a chromatin remodeling reaction and provides insights into how histone variants and nucleosome turnover can be controlled by chromatin regulators.

2013-04-15 | GSE43935 | GEO

Isw1 and Chd1 maintain chromatin organization during transcription [K56ac data]

Project description:ChIP-chip assays to determine the occupancy of acetylated histone H3 K56 in wildtype, isw1, chd1, isw1 chd1 and ISW1[K227R] yeast. Two color experiment. ChIP/Input. K56ac data normalized to histone H3 and plotted as mutant over wildtype. Biological replicates=3. Please note that H3 data for YMS123-125 & YMS127 is part of the AcH4 file.

2012-07-24 | E-GEOD-36405 | biostudies-arrayexpress

Pol II chromatin immunoprecipitation in S. cerevisiae

Project description:In Saccharomyces cerevisiae short non-coding RNA (ncRNA) generated by RNA Polymerase II (Pol II) are terminated by the NRD complex consisting of Nrd1, Nab3 and Sen1. We now show that Pcf11, a component of the cleavage and polyadenylation complex (CPAC), is generally required for NRD-dependent transcription termination through the action of its CTD interacting domain (CID). Pcf11 localizes downstream of Nrd1 on NRD terminators, and its recruitment depends on Nrd1. Furthermore mutation of the Pcf11 CID results in Nrd1 retention on chromatin, delayed degradation of ncRNA and restricts Pol II CTD Ser2 phosphorylation and Sen1-Pol II interaction. Finally, the pcf11-13 and sen1-1 mutant phenotypes are very similar as both accumulate RNA:DNA hybrids and display Pol II pausing downstream of NRD terminators. We predict a mechanism whereby Nrd1 and Pcf11 exchange on chromatin facilitates Pol II pausing and CTD Ser2-P phosphorylation. This in turn promotes Sen1 activity that is required for NRD-dependent transcription termination in vivo. ChIP-seq with antibody against pol II in wild type and Pcf11 mutants: Pcf11-2, Pcf11-9 and Pcf11-13 grown at 25C and 37C along with input samples

2015-04-02 | E-GEOD-67483 | biostudies-arrayexpress

Chromatin remodelers Isw1 and Chd1 maintain chromatin structure during transcription by preventing histone exchange

Project description:This SuperSeries is composed of the following subset Series: GSE32042: Isw1 and Chd1 maintain chromatin organization during transcription GSE32043: Histone exchange in wildtype, isw1, chd1, isw1 chd1 and ioc4 yeast strains GSE32044: Histone H3 K36me3 in wildtype, isw1 and chd1 yeast strains GSE32045: Isw1 and Chd1 maintain chromatin organization during transcription [AcH4 data] GSE36405: Isw1 and Chd1 maintain chromatin organization during transcription [K56ac data] GSE37158: Isw1 and Chd1 maintain chromatin organization during transcription [isw1 chd1 mutant expression] Refer to individual Series

2012-07-24 | E-GEOD-32071 | biostudies-arrayexpress

Divergent residues within histone H3 define a unique chromatin structure in S. cerevisiae

Project description:Histones are among the most conserved proteins known, but organismal differences do exist. In this study we examined the contribution that divergent amino acids within histone H3 make to cell growth and chromatin structure in S. cerevisiae. We show that, while amino acids that define histone H3.3 are dispensable for yeast growth, substitution of residues within the histone H3 alpha 3 helix with the human counterparts results in a severe growth defect. Mutations within this domain also result in altered nucleosome positioning, both in vivo and in vitro, which is accompanied by increased preference for nucleosome favoring sequences. These results suggest that divergent amino acids within the histone H3 alpha 3 helix play organismal roles in defining chromatin structure. Mnase-seq for two replicates each of wildtype and H3 c-terminal mutants.

2015-11-10 | E-GEOD-73425 | biostudies-arrayexpress

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